Abstract

FTIR spectroscopy has been used for the first time to investigate the kinetics of secondary structure formation during the refolding of small globular proteins. The refolding process was induced either by applying a temperature jump on the thermally denatured protein or by rapid dilution of a high concentrated denaturant solution containing the chemically unfolded protein. The experiments were carried out with Ribonuclease A (RNase A) as model system. The dead time of injection and the time resolution of the FTIR spectrometer permitted the observation of refolding kinetics in a time window ranging from milliseconds to several minutes and even hours.

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